Structure-function relationship in hemoproteins: The role of cytochromec3in the reduction of colloidal sulfur by sulfate-reducing bacteria
✍ Scribed by Guy Fauque; Denis Herve; Jean Gall
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 347 KB
- Volume
- 121
- Category
- Article
- ISSN
- 0302-8933
No coin nor oath required. For personal study only.
✦ Synopsis
Cytochromes c3 of different strains of sulfatereducing bacteria have been purified and tested for their capacity to reduce colloidal sulfur to hydrogen sulfide. The results are in good agreement with the activities reported for the whole cells. Cytochrome c3 is the sulfur reductase of some strains of sulfate-reducing bacteria such as DesulJbvibrio desulfuricans Norway 4 and sulfate-reducing bacterium strain 9974 from which the sulfur reductase activity can be purified with the cytochrome c3. In contrast, Desulfovibrio vulgaris Hildenborough cytochrome c3 is inhibited by the product of the reaction namely hydrogen sulfide. Chloramphenicol has no effect on the sulfur reductase activity of D. desulfuricans Norway 4 when resting cells grown on lactate-sulfate medium are put in the presence of colloidal sulfur. This shows that the sulfur reductase activity is constitutive and corresponds to the fact that colloidal sulfur grown cells do not contain more cytochrome c3 (or another sulfur reductase) than lactate-sulfate-grown cells.